Alpha-n-benzoylarginine-2-naphthylamide-amidohydrolase activity in chicken liver

F. Barceló
N. Vives
J. Bozal
44

Abstract

The enzyme activity from chicken liver that hydrolizes alpha-N-benzoil-DL-arginine-2-naphthylamide (BANA) has been separated into three active fractions by chromatography on Sephadex G-100 and DEAE-cellulose.The enzyme in Fraction FEA has a molecular weight greater than or equal to 100,000.The other two enzymes in Fractions FE1B and FE2B have a molecular weight around 23,000 and are separated by DEAE-cellulose chromatography.The BANA-hydrolase of fraction FE2B is unstable at pH alkaline and activates trypsinogen, in contrast with the enzyme of fraction FEB1.Both are thiol enzymes which behave analogously against activators (cysteine, dithiotreitol and 2-mercaptoethanol) and inhibitors (PCMB, IAA, N-ethylmaleimide, Cu2+, Hg2+ and Zn2+).

Keywords:
Cathepsins, Cysteine Endopeptidases, Aminopeptidases/metabolism, Animals, Benzoylarginine-2-Naphthylamide/metabolism, Cathepsin H, Chickens, Liver/enzymology

Authors

F. Barceló
N. Vives
J. Bozal


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